GLE1_HUMAN
ID GLE1_HUMAN Reviewed; 698 AA.
AC Q53GS7; O75458; Q53GT9; Q5VVU1; Q8NCP6; Q9UFL6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=mRNA export factor GLE1 {ECO:0000303|PubMed:14645504};
DE Short=hGLE1 {ECO:0000303|PubMed:9618489};
DE AltName: Full=GLE1 RNA export mediator {ECO:0000303|PubMed:18204449, ECO:0000312|HGNC:HGNC:4315};
DE AltName: Full=GLE1-like protein {ECO:0000305};
DE AltName: Full=Nucleoporin GLE1 {ECO:0000305};
GN Name=GLE1; Synonyms=GLE1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9618489; DOI=10.1073/pnas.95.12.6779;
RA Watkins J.L., Murphy R., Emtage J.L.T., Wente S.R.;
RT "The human homologue of Saccharomyces cerevisiae Gle1p is required for
RT poly(A)+ RNA export.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:6779-6784(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASP-130
RP AND GLN-590.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-698 (ISOFORM 1).
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12668658; DOI=10.1083/jcb.200211081;
RA Kendirgi F., Barry D.M., Griffis E.R., Powers M.A., Wente S.R.;
RT "An essential role for hGle1 nucleocytoplasmic shuttling in mRNA export.";
RL J. Cell Biol. 160:1029-1040(2003).
RN [7]
RP INTERACTION WITH NUP155.
RX PubMed=14645504; DOI=10.1074/mcp.m300106-mcp200;
RA Rayala H.J., Kendirgi F., Barry D.M., Majerus P.W., Wente S.R.;
RT "The mRNA export factor human Gle1 interacts with the nuclear pore complex
RT protein Nup155.";
RL Mol. Cell. Proteomics 3:145-155(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH NUP42 AND NUP155.
RX PubMed=16000379; DOI=10.1091/mbc.e04-11-0998;
RA Kendirgi F., Rexer D.J., Alcazar-Roman A.R., Onishko H.M., Wente S.R.;
RT "Interaction between the shuttling mRNA export factor Gle1 and the
RT nucleoporin hCG1: a conserved mechanism in the export of Hsp70 mRNA.";
RL Mol. Biol. Cell 16:4304-4315(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-88, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP VARIANTS LCCS1 PRO-PHE-GLN-144 INS AND HIS-569, VARIANTS CAAHD MET-617 AND
RP THR-684, AND CHARACTERIZATION OF VARIANT LCCS1 PRO-PHE-GLN-144 INS.
RX PubMed=18204449; DOI=10.1038/ng.2007.65;
RA Nousiainen H.O., Kestilae M., Pakkasjaervi N., Honkala H., Kuure S.,
RA Tallila J., Vuopala K., Ignatius J., Herva R., Peltonen L.;
RT "Mutations in mRNA export mediator GLE1 result in a fetal motoneuron
RT disease.";
RL Nat. Genet. 40:155-157(2008).
CC -!- FUNCTION: Required for the export of mRNAs containing poly(A) tails
CC from the nucleus into the cytoplasm. May be involved in the terminal
CC step of the mRNA transport through the nuclear pore complex (NPC).
CC {ECO:0000269|PubMed:12668658, ECO:0000269|PubMed:16000379,
CC ECO:0000269|PubMed:9618489}.
CC -!- SUBUNIT: Associated with the NPC, it however may not be a stable
CC component of the NPC complex since it shuttles between the nucleus and
CC the cytoplasm. Interacts with nuclear pore complex proteins NUP155 and
CC NUP42. Isoform 2 does not interact with NUP42. Able to form a
CC heterotrimer with NUP155 and NUP42 in vitro.
CC {ECO:0000269|PubMed:14645504, ECO:0000269|PubMed:16000379}.
CC -!- INTERACTION:
CC Q53GS7; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-1955541, EBI-14199987;
CC Q53GS7; Q9UII2: ATP5IF1; NbExp=3; IntAct=EBI-1955541, EBI-718459;
CC Q53GS7; Q16520: BATF; NbExp=3; IntAct=EBI-1955541, EBI-749503;
CC Q53GS7; Q00994: BEX3; NbExp=3; IntAct=EBI-1955541, EBI-741753;
CC Q53GS7; P24863: CCNC; NbExp=3; IntAct=EBI-1955541, EBI-395261;
CC Q53GS7; Q8NHQ1-3: CEP70; NbExp=3; IntAct=EBI-1955541, EBI-11526150;
CC Q53GS7; P51798: CLCN7; NbExp=3; IntAct=EBI-1955541, EBI-4402346;
CC Q53GS7; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-1955541, EBI-350590;
CC Q53GS7; Q9UER7: DAXX; NbExp=3; IntAct=EBI-1955541, EBI-77321;
CC Q53GS7; O00303: EIF3F; NbExp=2; IntAct=EBI-1955541, EBI-711990;
CC Q53GS7; Q8TAG9: EXOC6; NbExp=3; IntAct=EBI-1955541, EBI-1223394;
CC Q53GS7; P58499: FAM3B; NbExp=3; IntAct=EBI-1955541, EBI-12955347;
CC Q53GS7; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-1955541, EBI-8468186;
CC Q53GS7; O15287: FANCG; NbExp=3; IntAct=EBI-1955541, EBI-81610;
CC Q53GS7; P06241-3: FYN; NbExp=3; IntAct=EBI-1955541, EBI-10691738;
CC Q53GS7; Q9NS71: GKN1; NbExp=3; IntAct=EBI-1955541, EBI-3933251;
CC Q53GS7; Q53GS7: GLE1; NbExp=5; IntAct=EBI-1955541, EBI-1955541;
CC Q53GS7; O75409: H2AP; NbExp=3; IntAct=EBI-1955541, EBI-6447217;
CC Q53GS7; P26439: HSD3B2; NbExp=3; IntAct=EBI-1955541, EBI-21761225;
CC Q53GS7; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-1955541, EBI-9091197;
CC Q53GS7; Q8WYH8-2: ING5; NbExp=3; IntAct=EBI-1955541, EBI-21602071;
CC Q53GS7; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-1955541, EBI-714379;
CC Q53GS7; Q8IYD9: LAS2; NbExp=3; IntAct=EBI-1955541, EBI-749878;
CC Q53GS7; Q68G74: LHX8; NbExp=3; IntAct=EBI-1955541, EBI-8474075;
CC Q53GS7; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-1955541, EBI-741835;
CC Q53GS7; Q9UBF1: MAGEC2; NbExp=3; IntAct=EBI-1955541, EBI-5651487;
CC Q53GS7; P27338: MAOB; NbExp=3; IntAct=EBI-1955541, EBI-3911344;
CC Q53GS7; Q9Y483-4: MTF2; NbExp=3; IntAct=EBI-1955541, EBI-10698053;
CC Q53GS7; O76041: NEBL; NbExp=3; IntAct=EBI-1955541, EBI-2880203;
CC Q53GS7; Q16621: NFE2; NbExp=3; IntAct=EBI-1955541, EBI-726369;
CC Q53GS7; Q9Y239: NOD1; NbExp=3; IntAct=EBI-1955541, EBI-1051262;
CC Q53GS7; A5D8V7: ODAD3; NbExp=3; IntAct=EBI-1955541, EBI-8466445;
CC Q53GS7; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-1955541, EBI-1058491;
CC Q53GS7; Q9BR81: PCDHGC3; NbExp=3; IntAct=EBI-1955541, EBI-22012354;
CC Q53GS7; Q29RF7-3: PDS5A; NbExp=3; IntAct=EBI-1955541, EBI-12067280;
CC Q53GS7; O75925: PIAS1; NbExp=3; IntAct=EBI-1955541, EBI-629434;
CC Q53GS7; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-1955541, EBI-438710;
CC Q53GS7; Q96EN9: REX1BD; NbExp=3; IntAct=EBI-1955541, EBI-745810;
CC Q53GS7; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-1955541, EBI-3918154;
CC Q53GS7; Q96D59: RNF183; NbExp=3; IntAct=EBI-1955541, EBI-743938;
CC Q53GS7; Q969K3: RNF34; NbExp=3; IntAct=EBI-1955541, EBI-2340642;
CC Q53GS7; Q12824: SMARCB1; NbExp=3; IntAct=EBI-1955541, EBI-358419;
CC Q53GS7; O60641-3: SNAP91; NbExp=3; IntAct=EBI-1955541, EBI-12854506;
CC Q53GS7; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-1955541, EBI-7082156;
CC Q53GS7; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-1955541, EBI-357085;
CC Q53GS7; O75558: STX11; NbExp=3; IntAct=EBI-1955541, EBI-714135;
CC Q53GS7; P54274-2: TERF1; NbExp=3; IntAct=EBI-1955541, EBI-711018;
CC Q53GS7; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-1955541, EBI-12833746;
CC Q53GS7; O60220: TIMM8A; NbExp=3; IntAct=EBI-1955541, EBI-1049822;
CC Q53GS7; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-1955541, EBI-11525489;
CC Q53GS7; Q99598: TSNAX; NbExp=3; IntAct=EBI-1955541, EBI-742638;
CC Q53GS7; O75379-2: VAMP4; NbExp=3; IntAct=EBI-1955541, EBI-10187996;
CC Q53GS7; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-1955541, EBI-358545;
CC Q53GS7; Q9Y2L8: ZKSCAN5; NbExp=3; IntAct=EBI-1955541, EBI-2876965;
CC Q53GS7; Q8N895: ZNF366; NbExp=3; IntAct=EBI-1955541, EBI-2813661;
CC Q53GS7; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-1955541, EBI-8490788;
CC Q53GS7; Q86V28; NbExp=3; IntAct=EBI-1955541, EBI-10259496;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12668658}. Cytoplasm
CC {ECO:0000269|PubMed:12668658}. Note=Shuttles between the nucleus and
CC the cytoplasm (PubMed:12668658). Shuttling is essential for its mRNA
CC export function (PubMed:12668658). {ECO:0000269|PubMed:12668658}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:12668658}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:12668658}. Note=Shuttles between the nucleus and
CC the cytoplasm (PubMed:12668658). In the nucleus, isoform 1 localizes to
CC the nuclear pore complex and nuclear envelope (PubMed:12668658).
CC Shuttling is essential for its mRNA export function (PubMed:12668658).
CC {ECO:0000269|PubMed:12668658}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=hGle1B;
CC IsoId=Q53GS7-1; Sequence=Displayed;
CC Name=2; Synonyms=hGle1A;
CC IsoId=Q53GS7-2; Sequence=VSP_016486, VSP_016487;
CC -!- DISEASE: Lethal congenital contracture syndrome 1 (LCCS1) [MIM:253310]:
CC A form of lethal congenital contracture syndrome, an autosomal
CC recessive disorder characterized by degeneration of anterior horn
CC neurons, extreme skeletal muscle atrophy, and congenital non-
CC progressive joint contractures (arthrogryposis). The contractures can
CC involve the upper or lower limbs and/or the vertebral column, leading
CC to various degrees of flexion or extension limitations evident at
CC birth. LCCS1 patients manifest early fetal hydrops and akinesia,
CC micrognathia, pulmonary hypoplasia, pterygia, and multiple joint
CC contractures. It leads to prenatal death.
CC {ECO:0000269|PubMed:18204449}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Congenital arthrogryposis with anterior horn cell disease
CC (CAAHD) [MIM:611890]: An autosomal recessive disorder characterized by
CC fetal akinesia, arthrogryposis and motor neuron loss. The fetus often
CC survives delivery, but dies early as a result of respiratory failure.
CC Neuropathological findings resemble those of lethal congenital
CC contracture syndrome type 1, but are less severe.
CC {ECO:0000269|PubMed:18204449}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- SIMILARITY: Belongs to the GLE1 family. {ECO:0000305}.
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DR EMBL; AF058922; AAC25561.1; -; mRNA.
DR EMBL; AK222842; BAD96562.1; -; mRNA.
DR EMBL; AK222854; BAD96574.1; -; mRNA.
DR EMBL; AL445287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030012; AAH30012.1; -; mRNA.
DR EMBL; AL117584; CAB56006.1; -; mRNA.
DR CCDS; CCDS35154.1; -. [Q53GS7-1]
DR CCDS; CCDS6904.1; -. [Q53GS7-2]
DR PIR; T17316; T17316.
DR RefSeq; NP_001003722.1; NM_001003722.1. [Q53GS7-1]
DR RefSeq; NP_001490.1; NM_001499.2. [Q53GS7-2]
DR PDB; 6B4F; X-ray; 2.81 A; A/B=382-698.
DR PDB; 6B4I; X-ray; 3.62 A; A/B=382-698.
DR PDB; 6B4J; X-ray; 3.40 A; A/B=382-698.
DR PDBsum; 6B4F; -.
DR PDBsum; 6B4I; -.
DR PDBsum; 6B4J; -.
DR AlphaFoldDB; Q53GS7; -.
DR SMR; Q53GS7; -.
DR BioGRID; 108995; 155.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR CORUM; Q53GS7; -.
DR IntAct; Q53GS7; 75.
DR STRING; 9606.ENSP00000308622; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR iPTMnet; Q53GS7; -.
DR PhosphoSitePlus; Q53GS7; -.
DR BioMuta; GLE1; -.
DR DMDM; 83288218; -.
DR EPD; Q53GS7; -.
DR jPOST; Q53GS7; -.
DR MassIVE; Q53GS7; -.
DR MaxQB; Q53GS7; -.
DR PaxDb; Q53GS7; -.
DR PeptideAtlas; Q53GS7; -.
DR PRIDE; Q53GS7; -.
DR ProteomicsDB; 62487; -. [Q53GS7-1]
DR ProteomicsDB; 62488; -. [Q53GS7-2]
DR Antibodypedia; 31163; 212 antibodies from 31 providers.
DR DNASU; 2733; -.
DR Ensembl; ENST00000309971.9; ENSP00000308622.5; ENSG00000119392.16. [Q53GS7-1]
DR Ensembl; ENST00000372770.4; ENSP00000361856.4; ENSG00000119392.16. [Q53GS7-2]
DR GeneID; 2733; -.
DR KEGG; hsa:2733; -.
DR MANE-Select; ENST00000309971.9; ENSP00000308622.5; NM_001003722.2; NP_001003722.1.
DR UCSC; uc004bvi.4; human. [Q53GS7-1]
DR CTD; 2733; -.
DR DisGeNET; 2733; -.
DR GeneCards; GLE1; -.
DR HGNC; HGNC:4315; GLE1.
DR HPA; ENSG00000119392; Low tissue specificity.
DR MalaCards; GLE1; -.
DR MIM; 253310; phenotype.
DR MIM; 603371; gene.
DR MIM; 611890; phenotype.
DR neXtProt; NX_Q53GS7; -.
DR OpenTargets; ENSG00000119392; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 53696; Arthrogryposis-anterior horn cell disease syndrome.
DR Orphanet; 1486; Lethal congenital contracture syndrome type 1.
DR PharmGKB; PA28718; -.
DR VEuPathDB; HostDB:ENSG00000119392; -.
DR eggNOG; KOG2412; Eukaryota.
DR GeneTree; ENSGT00390000012903; -.
DR HOGENOM; CLU_024662_1_0_1; -.
DR InParanoid; Q53GS7; -.
DR OMA; FWKLLPD; -.
DR OrthoDB; 379050at2759; -.
DR PhylomeDB; Q53GS7; -.
DR TreeFam; TF324158; -.
DR PathwayCommons; Q53GS7; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR SignaLink; Q53GS7; -.
DR SIGNOR; Q53GS7; -.
DR BioGRID-ORCS; 2733; 470 hits in 1090 CRISPR screens.
DR ChiTaRS; GLE1; human.
DR GeneWiki; GLE1L; -.
DR GenomeRNAi; 2733; -.
DR Pharos; Q53GS7; Tbio.
DR PRO; PR:Q53GS7; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q53GS7; protein.
DR Bgee; ENSG00000119392; Expressed in buccal mucosa cell and 182 other tissues.
DR Genevisible; Q53GS7; HS.
DR GO; GO:0005814; C:centriole; IDA:CACAO.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0036064; C:ciliary basal body; IDA:CACAO.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0006449; P:regulation of translational termination; IBA:GO_Central.
DR Gene3D; 1.25.40.510; -; 1.
DR InterPro; IPR012476; GLE1.
DR InterPro; IPR038506; GLE1-like_sf.
DR PANTHER; PTHR12960; PTHR12960; 1.
DR Pfam; PF07817; GLE1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Disease variant; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW Transport.
FT CHAIN 1..698
FT /note="mRNA export factor GLE1"
FT /id="PRO_0000204822"
FT REGION 1..29
FT /note="Interaction with NUP155"
FT REGION 63..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..483
FT /note="Mediates the shuttling between the nucleus and the
FT cytoplasm"
FT REGION 656..698
FT /note="Interaction with NUP42"
FT /evidence="ECO:0000269|PubMed:16000379"
FT COILED 151..277
FT /evidence="ECO:0000255"
FT COILED 305..356
FT /evidence="ECO:0000255"
FT COMPBIAS 63..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 656..659
FT /note="IEAI -> YQAC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9618489, ECO:0000303|Ref.2"
FT /id="VSP_016486"
FT VAR_SEQ 660..698
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9618489, ECO:0000303|Ref.2"
FT /id="VSP_016487"
FT VARIANT 130
FT /note="G -> D (in dbSNP:rs17852725)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024056"
FT VARIANT 144
FT /note="T -> TPFQ (in LCCS1; allele Fin(Major); does not
FT affect subcellular localization)"
FT /evidence="ECO:0000269|PubMed:18204449"
FT /id="VAR_043874"
FT VARIANT 243
FT /note="I -> V (in dbSNP:rs2275260)"
FT /id="VAR_024057"
FT VARIANT 569
FT /note="R -> H (in LCCS1; dbSNP:rs121434407)"
FT /evidence="ECO:0000269|PubMed:18204449"
FT /id="VAR_043875"
FT VARIANT 590
FT /note="R -> Q (in dbSNP:rs17856852)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024058"
FT VARIANT 617
FT /note="V -> M (in CAAHD; dbSNP:rs121434408)"
FT /evidence="ECO:0000269|PubMed:18204449"
FT /id="VAR_043876"
FT VARIANT 684
FT /note="I -> T (in CAAHD; dbSNP:rs121434409)"
FT /evidence="ECO:0000269|PubMed:18204449"
FT /id="VAR_043877"
FT CONFLICT 83
FT /note="S -> P (in Ref. 2; BAD96574)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="F -> S (in Ref. 2; BAD96562)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="R -> G (in Ref. 2; BAD96562)"
FT /evidence="ECO:0000305"
FT HELIX 385..403
FT /evidence="ECO:0007829|PDB:6B4F"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 413..424
FT /evidence="ECO:0007829|PDB:6B4F"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 438..453
FT /evidence="ECO:0007829|PDB:6B4F"
FT STRAND 460..464
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:6B4J"
FT HELIX 470..490
FT /evidence="ECO:0007829|PDB:6B4F"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 499..512
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 514..527
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:6B4F"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 544..550
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 564..580
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 599..609
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 617..636
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 638..648
FT /evidence="ECO:0007829|PDB:6B4F"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 652..659
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 666..681
FT /evidence="ECO:0007829|PDB:6B4F"
FT HELIX 693..697
FT /evidence="ECO:0007829|PDB:6B4F"
SQ SEQUENCE 698 AA; 79836 MW; F9FC04683BCCDBB2 CRC64;
MPSEGRCWET LKALRSSDKG RLCYYRDWLL RREDVLEECM SLPKLSSYSG WVVEHVLPHM
QENQPLSETS PSSTSASALD QPSFVPKSPD ASSAFSPASP ATPNGTKGKD ESQHTESMVL
QSSRGIKVEG CVRMYELVHR MKGTEGLRLW QEEQERKVQA LSEMASEQLK RFDEWKELKQ
HKEFQDLREV MEKSSREALG HQEKLKAEHR HRAKILNLKL REAEQQRVKQ AEQERLRKEE
GQIRLRALYA LQEEMLQLSQ QLDASEQHKA LLKVDLAAFQ TRGNQLCSLI SGIIRASSES
SYPTAESQAE AERALREMRD LLMNLGQEIT RACEDKRRQD EEEAQVKLQE AQMQQGPEAH
KEPPAPSQGP GGKQNEDLQV KVQDITMQWY QQLQDASMQC VLTFEGLTNS KDSQAKKIKM
DLQKAATIPV SQISTIAGSK LKEIFDKIHS LLSGKPVQSG GRSVSVTLNP QGLDFVQYKL
AEKFVKQGEE EVASHHEAAF PIAVVASGIW ELHPRVGDLI LAHLHKKCPY SVPFYPTFKE
GMALEDYQRM LGYQVKDSKV EQQDNFLKRM SGMIRLYAAI IQLRWPYGNR QEIHPHGLNH
GWRWLAQILN MEPLSDVTAT LLFDFLEVCG NALMKQYQVQ FWKMLILIKE DYFPRIEAIT
SSGQMGSFIR LKQFLEKCLQ HKDIPVPKGF LTSSFWRS
